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Biomedical subjects

W Hong

Publications and source records attributed to W Hong.

At least 73 records · Page 4Linked to original sources

The reform of the rural cooperative medical system in the People's Republic of China: interim experience in 14 pilot counties.

During the 1960's and 1970's the Chinese government encouraged the 'rural cooperative medical systems' (RCMS), in order to ensure access to basic health care among the rural population. There was a break in the development of the RCMS in the early 1980's, as a consequence of market economic reforms. These reforms involved a shift from a communal to a household production system. As a result the collective way of financing rural health care was more or less abandoned. However, the government of the People's Republic of China was aware of the need to provide social protection against health care expenses. In March 1994 the government initiated a project to reestablish the RCMS. This project was implemented on a pilot basis in 14 counties of seven provinces. The reestablishment of the RCMS would be guided by the basic principles of health insurance. In October 1995, a first mid-term evaluation of the RCMS Project was held. One of the major research questions concerned the extent to which the RCMS had reduced the risk of paying health care bills that would otherwise be a burden on families. This article addresses this question and assesses the results obtained after two years of RCMS experimental work. A general finding is that the population structure by occupation and income varies, and that the RCMS has adapted itself to this variety. It is also confirmed that the burden of health care costs on families was reduced, more so in some counties than in others, but this reduction has been modest. The research results indicate that there is ample room for improvement. The outlook is hopeful, however. At the national level, there is now systematic thinking about RCMS. The current RCMS work is also having a considerable influence on other counties that are keen to reestablish the RCMS.

China↗

[Genetic polymorphism in natural populations of D. virilis].

In this paper we analysed the RFLP of mtDNA in Lanzhou (LZ) population of D. virilis. By reanalysing the RFLP data of our previous work on other natural populations of D. virilis, a phylogenetic tree was produced based on the UPGMA method. It shows three main clusters: the Northern populations (LZ QD), the East China populations (NJ, SH, NB) and the Southern population (QZ). With the mtDNA's RFLP data and the results of our former work on allozyme variation in natural populations of D. virilis, we suggest that there exists a latitudinal cline of genetic variation in natural populations of D.virilis. The mechanism for the maintenance of the observed latitudinal pattern is discussed.

Animals↗

[Expression of adhesion molecules beta 1 integrin on the surface of fibroblasts in wound healing].

OBJECTIVE: To investigate the relationship between the expression of adhesion molecules integrin beta 1 and the synthesis of collagen in wound healing. METHODS: In this study, integrin beta 1 expression on fibroblasts derived from granulated wound and from normal skin was compared by the technique of immunoelectron microscope and flow cytometry. The differences of ultrastructure between the two groups of fibroblasts were also observed. RESULTS: The results showed that the expression of alpha 5 and beta 1 subunits on fibroblasts derived from granulated wound were higher than those from normal skin. Endoplasmic reticulum attached with more ribosome in the former cells was richer than that in the latter cells. CONCLUSION: These results suggest that the expression of adhesion molecules integrin beta 1 appears to be associated with the synthesis of collagen in wound healing.

Adolescent↗

Effect of integrin on procollagen synthesis by fibroblasts from scleroderma.

OBJECTIVE: To investigate the effect of integrin on fibroblasts from scleroderma in the production of procollagen. METHODS: Phosphorothioate modified antisense oligonucleotides were used to interfere with the expression of integrin alpha 5 or beta 1 subunit on fibroblasts from 10 cases of scleroderma, and then the changes of procollagen mRNA due to the decline in level of integrin were observed by using RT-PCR. RESULTS: Expression of integrin alpha 5 or beta 1 subunit was specifically inhibited by their corresponding antisense oligonucleotides. Fibroblasts with decreased expression of alpha 5 or beta 1 subunit produced lower level of procollagen alpha 1 (I), alpha 1 (III) mRNA in comparison to the control. CONCLUSION: Overproduction of procollagen may be inhibited at the level of transcription by lowering the expression of integrin alpha 5 or beta 1 subunit on fibroblasts in scleroderma.

Adult↗

[A Raman spectral studies of rare-earth (REE) fluoro-carbonate minerals].

The Raman spectra of REE fluoro-carbonate minerals were studies by a type of RIT-30 laser Raman spectrometer. On the basis of Raman spectral properties, REE fluoro-carbonate minerals can be divided into three groups: Ba-REE fluoro-carbonate mineral, Ca-REE fluoro-carbonate mineral and REE fluoro-carbonate mineral. Obviously, a differential kind of mineral is different in the vibration frequency of the Raman spectra. They are as follows: Cordylite v1-1 088, v2-967, v3-1 538, v4-720, 628; Hauheite v1-1 089,v3-1 525, 1 596, v4-720, 649; Cerbaite v1-1 088, v2-911, v3-1 516, v4-718,625; Parisite v1-1 095,1 075, v2-915, v3-1 461, v4-744, 732; Bastnesite v1-1 098, v2-835, v3-1 476, 1 447, v4-732.

English Abstract↗

Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi transport.

Specific transport between secretory compartments requires that vesicular carriers contain targeting proteins known as SNAREs. Ten v-SNAREs have been identified in the genome of the yeast Saccharomyces cerevisiae by sequence analysis. We report here the characterization of Gos1p, a v-SNARE localized to the Golgi compartment and likely homolog of the mammalian protein GOS-28/GS28. Gos1p is a type II membrane protein with characteristic SNARE sequence hallmarks and is functionally a SNARE protein. Gos1p was originally identified as a 28 kDa protein in an immunoprecipitate of the cis-Golgi t-SNARE Sed5p. This interaction between Sed5p and Gos1p is direct as demonstrated by in vitro binding with recombinant proteins. Deletion of GOS1 results in viable haploids with modest growth and secretory defects. Close examination of the secretory phenotype of GOS1-disrupted cells suggests that Gos1p may play a role in multiple transport steps, specifically ER-Golgi and/or intra-Golgi transport.

Biological Transport↗

A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (Vti1-rp2) implicated in protein trafficking in the secretory pathway.

Expressed sequence tags coding for a potential SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) were revealed during data base searches. The deduced amino acid sequence of the complete coding region predicts a 217-residue protein with a COOH-terminal hydrophobic membrane anchor. Affinity-purified antibodies raised against the cytoplasmic region of this protein specifically detect a 29-kilodalton integral membrane protein enriched in the Golgi membrane. Indirect immunofluorescence microscopy reveals that this protein is mainly associated with the Golgi apparatus. When detergent extracts of the Golgi membrane are incubated with immobilized glutathione S-transferase alpha soluble N-ethylmaleimide-sensitive factor attachment protein (GST-alpha-SNAP), this protein was specifically retained. This protein has been independently identified and termed Vti1-rp2, and it is homologous to Vti1p, a yeast Golgi SNARE. We further show that Vti1-rp2 can be qualitatively coimmunoprecipitated with Golgi syntaxin 5 and syntaxin 6, suggesting that Vti1-rp2 exists in at least two distinct Golgi SNARE complexes. In cells microinjected with antibodies against Vti1-rp2, transport of the envelope protein (G-protein) of vesicular stomatitis virus from the endoplasmic reticulum to the plasma membrane was specifically arrested at the Golgi apparatus, providing further evidence for functional importance of Vti1-rp2 in protein trafficking in the secretory pathway.

Amino Acid Sequence↗

A single plasmid vector (pSTAR) mediating efficient tetracycline-induced gene expression.

A plasmid vector (pSTAR) has been constructed which confers neomycin resistance for selecting stably transfected cells, possesses a cloning cassette for placing a gene of interest under the control of the tetO DNA motif, and expresses rtTAnls which, upon association with tetracycline, binds to and drives gene expression from the tetO DNA motif. The plasmid pSTAR/LacZ, which has the gene for beta-galactosidase inserted into the cloning cassette, was transfected into Chinese hamster ovary (CHO) cells and selected for stably transfected cells. In pooled transfectants of CHO, tetracycline induced the expression of beta-galactosidase in 10-30% of cells. Using clonal transfectants, beta-galactosidase expression was induced by tetracycline in essentially every cell. Furthermore, induction of beta-galactosidase expression by tetracycline was both dose- and time-dependent. Similar tetracycline-induced beta-galactosidase expression is also observed in other cell types. The pSTAR vector is thus suited to facilitate the application of tetracycline-induced gene expression in diverse research areas.

Animals↗

Syntaxin 11: a member of the syntaxin family without a carboxyl terminal transmembrane domain.

We have cloned a novel syntaxin-like molecule, designated human syntaxin 11 (hsyn11). The open reading frame encodes a polypeptide of 287 amino acids with potential coiled-coil domains. hsyn11 has extensive homology to members of the syntaxin family, particularly syntaxin 1 and syntaxin 2. Unlike other members of the syntaxin family, however, hsyn11 has a short cysteinerich carboxyl-terminal tail but not a typical hydrophobic domain which may serve as a membrane anchor. Northern blot analysis revealed two transcripts of approximately 0.8 kb and approximately 1.7 kb in length that are particularly abundant in heart and placenta, although lower levels were also detectable in other tissues except in the brain. Consistent with the lack of a distinct membrane anchorage sequence in hsyn11, indirect immunofluorescence microscopy of transiently expressed N-terminally myc-tagged hsyn11 revealed a diffuse, cytoplasmic labeling.

Amino Acid Sequence↗

Syntaxin 12, a member of the syntaxin family localized to the endosome.

We have cloned a new member of the syntaxin family of proteins. The open reading frame encodes a polypeptide of 272 amino acids with potential coiled-coil domains and a C-terminal hydrophobic tail. Northern blot analysis showed that the transcript is fairly ubiquitous. A soluble recombinant form of the polypeptide without the hydrophobic region binds to alpha-SNAP (soluble N-ethylmaleimide-sensitive factor attachment protein) and syndet/SNAP-23 in vitro. Polyclonal antibody raised against the recombinant protein recognized a 39-kDa protein in the membrane fraction of cell lysates. Indirect immunofluorescence studies using the polyclonal antibody showed that the protein is localized to intracellular membrane structures. Selective permeabilization studies with digitonin and saponin indicate that the epitope(s) recognized by the antibody is expose to the cytoplasm, consistent with the predicted orientation characteristic of SNAP receptor molecules. Morphological alterations of the staining pattern of the protein with brefeldin A and wortmannin treatment indicate that the protein is localize to the endosome. The cDNA we have cloned apparently corresponded to three previously described expressed sequence tags named as syntaxins 12, 13, and 14, respectively. We therefore propose to retain the name syntaxin 12 for this protein.

Amino Acid Sequence↗

Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1.

Protein tyrosine phosphatases (PTPs) play a fundamental role in regulating diverse cellular processes. PRL-1 is a unique nuclear PTP that is induced in mitogen-stimulated cells and regenerating liver. Database searches using the PRL-1 sequence led to the identification of mouse PRL-2 and PRL-3 which exhibit 87% and 76% identity to mouse PRL-1 in their amino acid sequences. All three mouse PRL proteins contain a C-terminal consensus sequence for prenylation. All PRL proteins bear significant sequence homology to Cdc14p and the recently identified tumor suppressor PTEN/MMAC1, in regions other than the conserved PTP signature motif. The nucleotide sequences of the coding regions of mouse PRL-2 and PRL-3 are, respectively, 71% and 62%, identical to mouse PRL-1, while the 5' un-translated regions of mouse PRL-1, PRL-2, and PRL-3 are much more divergent. Northern blot analysis revealed that PRL-2 is preferentially expressed in skeletal muscle, while PRL-3 is preferentially expressed in both skeletal muscle and heart, although both PRL-2 and PRL-3 are expressed at lower levels in other tissues.

Amino Acid Sequence↗

Hsec22c: a homolog of yeast Sec22p and mammalian rsec22a and msec22b/ERS-24.

We have cloned a new member of a family of mammalian proteins homologous to Sec22p, a v-SNARE in Saccharomyces cerevisiae required for transport between the endoplasmic reticulum (ER) and the Golgi apparatus. The open reading frame encodes a polypeptide of 250 amino acids which is homologous to, but obviously different from, the recently reported mammalian Sec22p homologs rat sec22a, mouse sec22b, and hamster ERS-24. Northern blot analysis revealed two transcripts of about 1 and 5 kb respectively which are ubiquitously expressed. myc-epitope tagged sec22c is localized to the ER. Overexpression of the myc-tagged protein resulted in an anomalous staining pattern of SNARE molecules participating in ER-Golgi transport such as syntaxin 5 and mammalian bet1, but not the endosomal SNARE syntaxin 7. The presence of multiple forms of sec22 protein in the mammalian early secretory pathway is in-line with task specification in a highly elaborate transport machinery.

Amino Acid Sequence↗

Molecular cloning and localization of human syntaxin 16, a member of the syntaxin family of SNARE proteins.

We have cloned a new member of the syntaxin family of proteins, designated human syntaxin 16 (hsyn16). The open reading frame encodes a polypeptide of 307 amino acids with potential coiled-coil domains and a carboxy-terminal hydrophobic tail, which is characteristic of other members of the syntaxin family. The encoded polypeptide bears sequence homology to known syntaxin molecules. Northern blot analysis revealed a single transcript that is fairly ubiquitous, being slightly more enriched in heart and pancreas. Indirect immunofluorescence localised myc-tagged hsyn16 (myc-hsyn16) to the Golgi apparatus, colocalizing well with lens culinaris agglutinin, an established Golgi marker, as well as with other Golgi SNAREs such as GS28 and syntaxin 5. Myc-hsyn16 is redistributed to the endoplasmic reticulum upon brefeldin A treatment, indicating that it is localised to the Golgi stack. The ubiquitous expression and Golgi localization of hsy16 suggest that it is involved in a vesicular transport step within the organelle.

Amino Acid Sequence↗

Syntaxin 10: a member of the syntaxin family localized to the trans-Golgi network.

We have cloned a new member of the syntaxin family of proteins, designated human syntaxin 10 (hsyn10). The open reading frame encodes a polypeptide of 249 amino acids with potential coiled-coil domains and a carboxy-terminal hydrophobic tail. hsyn10 is particularly homologous to the recently reported rat syntaxin 6 (about 60% identity). Northern blot analysis showed that the transcript is enriched in the heart, skeletal muscles and pancreas. Indirect immunofluorescence studies using polyclonal antibodies raised against recombinant protein showed that the protein is localized to intracellular membrane structures, with perinuclear staining patterns colocalising well with the Golgi SNARE GS28. Morphological alterations of the staining pattern of the protein with brefeldin A but not wortmannin treatment indicate that the protein is localize to the trans-Golgi network.

Amino Acid Sequence↗

Syntaxin 7, a novel syntaxin member associated with the early endosomal compartment.

Members of the syntaxin family are key molecules involved in diverse vesicle docking/fusion events. We report here the molecular, biochemical, and cell biological characterizations of a novel member (syntaxin 7) of the syntaxin family. Syntaxin 7 is structurally related to all known syntaxins. Within a 79-residue region preceding the C-terminal hydrophobic tail, syntaxin 7 is 35, 34, 34, 34, 25, and 19% identical to syntaxins 1, 2, 3, 4, 5, and 6, respectively. Northern blot analysis showed that syntaxin 7 is widely expressed. Indirect immunofluorescence microscopy revealed that syntaxin 7 is primarily associated with the early endosome. In vitro binding assays established that syntaxin 7 in membrane extracts interacts with immobilized recombinant alpha-soluble N-ethylmaleimide-sensitive factor attachment proteins fused to glutathione S-transferase. Our results highlight the general importance of members of the syntaxin family in protein trafficking and provide new avenues for future functional and mechanistic studies of this first endosomal syntaxin as well as the endocytotic pathway.

Amino Acid Sequence↗

Inhibins, activins, and follistatins: expression of mRNAs and cellular localization in tissues from men with benign prostatic hyperplasia.

BACKGROUND: The transforming growth factor beta (TGF beta) superfamily of growth factors includes activins and inhibins, which have been shown to be present in the rat ventral prostate, and human prostate tumor cell lines, although their localization in benign prostatic hyperplasia (BPH) tissue is currently unknown. METHODS: BPH tissues were obtained at surgery, and the mRNA expression for the inhibin alpha, beta A, beta B subunits, the putative activin beta C subunit, the activin type II receptor (ActRII), and the activin binding protein, follistatin, was determined by reverse transcription polymerase chain reaction (RT-PCR) and Southern blot analysis. Antibodies specific for alpha, beta A, beta B, activin A, and follistatin were used to determine the localization of these proteins in BPH tissue specimens. RESULTS: Southern blot analysis confirmed that mRNA for ActRII, beta C subunit, and follistatin was present in all biopsy samples assayed. However, alpha, beta A, and beta B subunit mRNA expression was variable between patient samples. Immunohistochemistry demonstrated the predominant localization of beta A, beta B, and activin A proteins to the epithelium of BPH tissues. No immunoreactivity for the inhibin alpha subunit was detected; follistatin immunoreactivity was localized to the fibroblastic stroma. CONCLUSIONS: The compartmentalization of activin subunit proteins to the epithelium, and of follistatin to the stroma, suggests that a paracrine interaction occurs between the activin ligands and follistatin-binding proteins in BPH tissue.

Activin Receptors↗

Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome.

Synaptobrevins/vesicle-associated membrane proteins (VAMPs) together with syntaxins and a synaptosome-associated protein of 25 kDa (SNAP-25) are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. We report here the molecular, biochemical, and cell biological characterization of a novel member of the synaptobrevin/VAMP family. The amino acid sequence of endobrevin has 32, 33, and 31% identity to those of synaptobrevin/VAMP-1, synaptobrevin/VAMP-2, and cellubrevin, respectively. Membrane fractionation studies demonstrate that endobrevin is enriched in membrane fractions that are also enriched in the asialoglycoprotein receptor. Indirect immunofluorescence microscopy establishes that endobrevin is primarily associated with the perinuclear vesicular structures of the early endocytic compartment. The preferential association of endobrevin with the early endosome was further established by electron microscopy (EM) immunogold labeling. In vitro binding assays show that endobrevin interacts with immobilized recombinant alpha-SNAP fused to glutathione S-transferase (GST). Our results highlight the general importance of members of the synaptobrevin/VAMP protein family in membrane traffic and provide new avenues for future functional and mechanistic studies of this protein as well as the endocytotic pathway.

Amino Acid Sequence↗